HIV-1 Matrix protein (MA)

The HIV-1 Matrix protein (MA), also known as p17, is a structural component of the Human Immunodeficiency Virus type 1, derived from the N-terminal region of the Gag polyprotein (UniProt: P04591). It plays a critical role in the viral life cycle by mediating the targeting and binding of the Gag precursor to the host cell's plasma membrane through its myristoylated N-terminus and a highly basic patch that interacts with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) (PubMed: 19158271). Beyond assembly, MA is involved in the incorporation of the viral envelope (Env) glycoproteins into budding particles and facilitates the nuclear import of the viral pre-integration complex in non-dividing cells (PubMed: 26861410). While not currently the target of any FDA-approved antiretroviral therapies, MA is an attractive target for drug development due to its essential roles in both early and late stages of infection (PubMed: 31481552). Experimental small molecules, such as L-64, aim to disrupt its membrane association or its interaction with Env, potentially offering a new class of inhibitors to combat multi-drug resistant HIV strains (PubMed: 21106747).

Other names

p17Gag p17Matrix protein p17HIV-1 MA

Inhibition of the interaction between the matrix protein and the host cell plasma membrane, specifically targeting the binding to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), or disrupting the incorporation of the envelope glycoprotein into nascent virions (PubMed: 31481552).